Succinyl phosphonate inhibits alpha-ketoglutarate oxidative decarboxylation, catalyzed by alpha-ketoglutarate dehydrogenase complexes from E-coli and pigeon breast muscle

被引：22
作者：
Biryukov, AI
Bunik, VI
Zhukov, YN
Khurs, EN
Khomutov, RM
机构：
[1] RUSSIAN ACAD SCI, VA ENGELHARDT MOLEC BIOL INST, MOSCOW 117984, RUSSIA
[2] MOSCOW MV LOMONOSOV STATE UNIV, DEPT BIOL, CHAIR BIOCHEM, MOSCOW, RUSSIA
来源：
FEBS LETTERS | 1996年 / 382卷 / 1-2期
关键词：
alpha-ketoglutarate dehydrogenase; alpha-ketoglutarate phosphoanalogue; glutamate phosphoanalogue; E-coli extract; transamination;
D O I：
10.1016/0014-5793(96)00166-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Effects of a set of a-ketoglutarate phosphoanalogues on the activity of alpha-ketoglutarate dehydrogenase (EC 1.2.4.2) complexes from E. coli and pigeon breast muscle, as well as on alpha-ketoglutarate dehydrogenase isolated from the pigeon breast muscle, have been studied, alpha-Ketoglutarate phosphoanalogues (succinyl phosphonate and its monomethyl ester) were found to be effective inhibitors of alpha-ketoglutarate oxidative decarboxylation, catalyzed by both muscle and bacterial alpha-ketoglutarate dehydrogenase complexes, as well as muscle alpha-ketoglutarate dehydrogenase, The ability of glutamate phosphoanalogues to inhibit alpha-ketoglutarate oxidative decarboxylation has been shown in E. coli extract and a model system.
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页码：167 / 170
页数：4
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